View source for 1bw6


==HUMAN CENTROMERE PROTEIN B (CENP-B) DNA BINDIGN DOMAIN RP1==
<StructureSection load='1bw6' size='340' side='right'caption='[[1bw6]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bw6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BW6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BW6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bw6 OCA], [https://pdbe.org/1bw6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bw6 RCSB], [https://www.ebi.ac.uk/pdbsum/1bw6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bw6 ProSAT], [https://www.topsan.org/Proteins/RSGI/1bw6 TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CENPB_HUMAN CENPB_HUMAN] Interacts with centromeric heterochromatin in chromosomes and binds to a specific subset of alphoid satellite DNA, called the CENP-B box. May organize arrays of centromere satellite DNA into a higher-order structure which then directs centromere formation and kinetochore assembly in mammalian chromosomes.
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== Publication Abstract from PubMed ==
CENP-B has been suggested to organize arrays of centromere satellite DNA into a higher order structure which then directs centromere formation and kinetochore assembly in mammalian chromosomes. The N-terminal portion of CENP-B is a 15 kDa DNA binding domain (DBD) consisting of two repeating units, RP1 and RP2. The DBD specifically binds to the CENP-B box sequence (17 bp) in centromere DNA. We determined the solution structure of human CENP-B DBD RP1 by multi-dimensional 1H, 13C and 15N NMR methods. The CENP-B DBD RP1 structure consists of four helices and has a helix-turn-helix structure. The overall folding is similar to those of some other eukaryotic DBDs, although significant sequence homology with these proteins was not found. The DBD of yeast RAP1, a telomere binding protein, is most similar to CENP-B DBD RP1. We studied the interaction between CENP-B DBD RP1 and the CENP-B box by the use of NMR chemical shift perturbation. The results suggest that CENP-B DBD RP1 interacts with one of the essential regions of the CENP-B box DNA, mainly at the N-terminal basic region, the N-terminal portion of helix 2 and helix 3.

A helix-turn-helix structure unit in human centromere protein B (CENP-B).,Iwahara J, Kigawa T, Kitagawa K, Masumoto H, Okazaki T, Yokoyama S EMBO J. 1998 Feb 2;17(3):827-37. PMID:9451007<ref>PMID:9451007</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1bw6" style="background-color:#fffaf0;"></div>

==See Also==
*[[Centromere protein 3D structure|Centromere protein 3D structure]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Iwahara J]]
[[Category: Kigawa T]]
[[Category: Kitagawa K]]
[[Category: Masumoto H]]
[[Category: Okazaki T]]
[[Category: Yokoyama S]]